Submitted to: National Center for Biotechnology Information (NCBI)
Publication Type: Other
Publication Acceptance Date: May 29, 2005
Publication Date: June 6, 2005
Citation: Hunter, W.B., Smith, M.T. 2005. Ferritin 2 and Muscular protein 20-like cDNA from Asian Longhorned Beetle 5th-instar larva. National Center for Biotechnology Information, NCBI. Accession Nos. DQ067275 and DQ067276. Interpretive Summary: The Asian Longhorn Beetle, ALB, Anoplophora glabripennis (Motschulsky) is an invasive insect that attacks and kills trees. ALB feeds on a wide variety of hardwood tree hosts in China and in the United States, including maples, elm, birch, willow, and popular. One study reported that larvae successfully fed on 23 species of poplar (Populus) and 24 other tree species in China ALB is a major forest pest in China, and in New York and Illinois has demonstrated formidable potential for harming many important commercial tree species in the forests of North America. ALB biology is now being studied from the inside-out through the use of molecular genetic techniques. To identify functional genes within ALB a gene expression library was produced and genes have been identified. Two of these Ferritin-2, a storage protein, and a muscle protein, mp20, have been completely sequenced. Storage proteins are important in insect development and act as an amino acid source during insect pupal and adult metamorphosis, and in reproduction. Muscle development and function are also critical to beetle development. Increasing our understanding of how these proteins function in ALB development permits researchers to develop better methods for use in the management of this devastating tree pest.
Technical Abstract: We describe here two proteins identified from an expression library made to larval Asian longhorn beetles, ALB, Anoplophora glabripennis (Motschulsky). Characterization of these two cDNA’s identified an arylphorin-like hexameric storage protein similar to the protein from the mulberry longicorn beetle, Apriona germari (Coleoptera, Cerambycidae). The complete cDNA sequence of the ALB storage protein is comprised of 1,998 bp with 666 amino acid residues. The second cDNA had significant similarity to muscle protein in Drosophila melanogaster encoding a muscle specific protein, mp20. The ALB mp20 is comprised of 1,665 bp, with 555 amino acid residues. The cDNA encodes a 20-kD protein, muscle protein 20 (mp20) that is found in most, if not all, other muscles (the synchronous muscles). The sequence of the protein, deduced from the DNA, contains two regions of 12 amino acids with significant similarity to high-affinity calcium-binding sites of other proteins. By increasing our understanding of how these proteins function in ALB development researchers will be able to develop better methods for use in the management of this devastating tree pest.